ID   MBEC_ECOLX              Reviewed;         115 AA.
AC   P13657;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Mobilization protein MbeC;
DE   AltName: Full=Conjugative accessory protein MbeC;
GN   Name=mbeC;
OS   Escherichia coli.
OG   Plasmid ColE1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2671664; DOI=10.1007/bf02464922;
RA   Boyd A.C., Archer J.A.K., Sherratt D.J.;
RT   "Characterization of the ColE1 mobilization region and its protein
RT   products.";
RL   Mol. Gen. Genet. 217:488-498(1989).
RN   [2]
RP   FUNCTION, DETERMINATION OF TRANSCRIPTIONAL START SITE, SUBUNIT, DOMAIN,
RP   MUTAGENESIS OF ARG-13, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19114496; DOI=10.1128/jb.01342-08;
RA   Varsaki A., Moncalian G., Garcillan-Barcia M.P., Drainas C., de la Cruz F.;
RT   "Analysis of ColE1 MbeC unveils an extended ribbon-helix-helix family of
RT   nicking accessory proteins.";
RL   J. Bacteriol. 191:1446-1455(2009).
CC   -!- FUNCTION: Required for efficient mobilization of ColE1 plasmid and is
CC       thus essential to promote the specific transfer of the plasmid during
CC       conjugation. Probably functions by inducing DNA bending, helping the
CC       MbeA relaxase to melt the DNA around the nic site and cleave the
CC       phosphodiester bond. Binds specifically double-stranded DNA (dsDNA)
CC       containing the ColE1 oriT but does not recognize the inverted repeat
CC       (IR). {ECO:0000269|PubMed:19114496}.
CC   -!- SUBUNIT: Homodimer. Interacts with MbeA and MbeB to form the
CC       relaxosome. {ECO:0000269|PubMed:19114496}.
CC   -!- INTERACTION:
CC       P13657; P13658: mbeA; NbExp=2; IntAct=EBI-7798318, EBI-7798346;
CC   -!- DOMAIN: Consists of two domains: the N-terminal domain, which contains
CC       a predicted ribbon-helix-helix (RHH) DNA-binding domain, and the C-
CC       terminal domain, which comprises a signature shared by nicking
CC       accessory proteins. {ECO:0000269|PubMed:19114496}.
CC   -!- SIMILARITY: To E.coli MbaC and MbkC. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA33882.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X15873; CAA33882.1; ALT_INIT; Genomic_DNA.
DR   PIR; JQ0389; JQ0389.
DR   RefSeq; NP_040368.1; NC_001371.1.
DR   RefSeq; WP_010889873.1; NC_025013.1.
DR   RefSeq; YP_009062852.1; NC_025013.1.
DR   AlphaFoldDB; P13657; -.
DR   SMR; P13657; -.
DR   IntAct; P13657; 1.
DR   MINT; P13657; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008687; MobC.
DR   Pfam; PF05713; MobC; 1.
PE   1: Evidence at protein level;
KW   Conjugation; DNA-binding; Mobility protein; Plasmid.
FT   CHAIN           1..115
FT                   /note="Mobilization protein MbeC"
FT                   /id="PRO_0000068402"
FT   MUTAGEN         13
FT                   /note="R->A: Unable to bind either single- or double-
FT                   stranded DNA. Reduces ColE1 mobilization by 3000-fold."
FT                   /evidence="ECO:0000269|PubMed:19114496"
SQ   SEQUENCE   115 AA;  12898 MW;  2776BC02394781F7 CRC64;
     MIPMKRERML TIRVTDDEHA RLLERCEGKQ LAVWMRRVCL GEPVARSGKL PTLAPPLLRQ
     LAAIGNNLNQ TARKVNSGQW SSGDRVQVVA ALMAIGDELR RLRLAVREQG ARDDS